Research

Research Interests

The Vincent group are interested in understanding details of catalysis and reactions at metal sites, both in enzymes and on metal nanoparticles relevant to fuel cell catalysis. Redox enzymes play key roles as catalysts in biological cycling of hydrogen, carbon and nitrogen and energy. Their active sites are built from common metals such as iron, nickel and copper, and the reactivity achieved at these centres is often difficult to replicate under ambient conditions with synthetic catalysts. We are interested in understanding details of the redox chemistry and mechanisms of catalysis occurring at enzyme active sites. A central theme in our research is attachment of enzymes to electrically conducting surfaces (electrodes or conducting particles). This provides precise control over enzyme reactions in direct electrochemical and spectroelectrochemical studies, but it also provides an immediate route to applying biological redox catalysis in hydrogen technologies and in specialised catalysis.

Our studies target a range of metalloproteins including hydrogenases, nitrogenase and nitric oxide sensing proteins. We are particularly interested in the efficient catalysis of H2 oxidation and production by microbial hydrogenase enzymes at [NiFe] active centres. Ligands at the active site of hydrogenases, CO and CN-, give rise to fairly intense absorption bands in the Infrared spectrum. This has inspired us to develop new approaches to infrared spectroelectrochemistry for studying hydrogenase active site chemistry under direct electrochemical control. Understanding and exploiting selective enzyme catalysis will provide inspiration for new hydrogen energy technologies and development of novel catalytic materials.

We have demonstrated and patented the HydRegen system for recycling the biological cofactors NAD(P)+ and NAD(P)H with H2 as electron source or sink using graphite particles modified with enzyme moieties. We are developing this further to support catalysis by a wide range of NAD(P)H dependent enzymes, including keto reductases, ene reductases and amino acid dehydrogenases, and are working in collaboration with industry to develop enzyme beads for industrial fine chemical synthesis.

Kylie Vincent's research is supported by the EPSRC, BBSRC and InnovateUK, and supported by collaboration with a variety of industrial partners including Johnson Matthey Catalysis and Chiral Technologies and Dr Reddy's.

Opportunities in the Vincent Group

Informal enquiries about Postdoctoral Fellowship applications, Graduate DPhil (PhD) or MSc opportunities or Undergraduate Summer Studentships in the group should be directed to Prof Kylie Vincent. General information about graduate studies at Oxford is available on the Oxford University Graduate Admissions Website. We are always happy to hear from candidates interested in applying for their own scholarship or fellowship funding to work in the group.

The Vincent group will take 3 Part II Oxford MChem students for 2018/2019. Email Kylie Vincent for further information about future Part II projects. Further information about the group is also available on the group webpages.